Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis

Biochem Biophys Res Commun. 2000 Feb 24;268(3):921-7. doi: 10.1006/bbrc.2000.2231.

Abstract

We have identified human and mouse peroxiredoxin V (Prx-V) by virtue of the sequence homologies to yeast peroxisomal antioxidant enzyme PMP20. Prx-V represents the fifth of the six currently known subfamilies of mammalian peroxiredoxins. It is a novel organellar enzyme that has orthologs in bacteria. Biochemically, Prx-V is a thioredoxin peroxidase. One important aspect of p53 function in mammalian cells involves induction of apoptosis likely mediated by redox. We show that overexpression of Prx-V prevented the p53-dependent generation of reactive oxygen species. Likewise, Prx-V inhibited p53-induced apoptosis. Thus, Prx-V is critically involved in intracellular redox signaling.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Apoptosis / drug effects*
  • Base Sequence
  • DNA Primers / genetics
  • Gene Expression
  • HeLa Cells
  • Humans
  • In Vitro Techniques
  • Mice
  • Molecular Sequence Data
  • Neoplasm Proteins*
  • Oxidation-Reduction
  • Peroxidases / genetics
  • Peroxidases / metabolism
  • Peroxidases / pharmacology*
  • Peroxiredoxin III
  • Peroxiredoxins
  • Phylogeny
  • Reactive Oxygen Species / metabolism
  • Sequence Homology, Amino Acid
  • Signal Transduction
  • Tumor Suppressor Protein p53 / metabolism
  • Tumor Suppressor Protein p53 / pharmacology*

Substances

  • DNA Primers
  • Neoplasm Proteins
  • Prdx3 protein, mouse
  • Reactive Oxygen Species
  • Tumor Suppressor Protein p53
  • Peroxidases
  • PRDX3 protein, human
  • PRDX5 protein, human
  • Peroxiredoxin III
  • Peroxiredoxins
  • Prdx5 protein, mouse